ACRBP_MOUSE
ID ACRBP_MOUSE Reviewed; 540 AA.
AC Q3V140; Q62253; Q62254; Q8C621; Q91VQ1;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Acrosin-binding protein;
DE AltName: Full=Acrosin-binding protein, 60 kDa form;
DE AltName: Full=Proacrosin-binding protein sp32;
DE Contains:
DE RecName: Full=Acrosin-binding protein, mature form;
DE AltName: Full=ACRPB-C {ECO:0000303|PubMed:23426433};
DE AltName: Full=Acrosin-binding protein, 32 kDa form, mature form;
DE AltName: Full=Sp32 {ECO:0000303|Ref.1};
DE Flags: Precursor;
GN Name=Acrbp {ECO:0000312|MGI:MGI:1859515};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAA04498.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=ddY {ECO:0000312|EMBL:BAA04498.1};
RC TISSUE=Testis {ECO:0000312|EMBL:BAA04498.1};
RA Baba T.;
RT "Rodent-specific alternative splicing of RNA for mammalian sperm
RT proacrosin-binding protein, sp32.";
RL Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAE21313.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE21313.1};
RC TISSUE=Testis {ECO:0000312|EMBL:BAE21313.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAH11079.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Mammary gland {ECO:0000312|EMBL:AAH11079.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=22357636; DOI=10.1093/molehr/gas009;
RA Tardif S., Guyonnet B., Cormier N., Cornwall G.A.;
RT "Alteration in the processing of the ACRBP/sp32 protein and sperm
RT head/acrosome malformations in proprotein convertase 4 (PCSK4) null mice.";
RL Mol. Hum. Reprod. 18:298-307(2012).
RN [6]
RP SUBCELLULAR LOCATION (ISOFORMS 1 AND 2), TISSUE SPECIFICITY (ISOFORMS 1 AND
RP 2), AND INTERACTION WITH ACR (ISOFORMS 1 AND 2).
RX PubMed=23426433; DOI=10.1095/biolreprod.112.107425;
RA Kanemori Y., Ryu J.H., Sudo M., Niida-Araida Y., Kodaira K., Takenaka M.,
RA Kohno N., Sugiura S., Kashiwabara S., Baba T.;
RT "Two functional forms of ACRBP/sp32 are produced by pre-mRNA alternative
RT splicing in the mouse.";
RL Biol. Reprod. 88:105-105(2013).
RN [7]
RP DISRUPTION PHENOTYPE, FUNCTION (ISOFORMS 1 AND 2), AND SUBCELLULAR LOCATION
RP (ISOFORMS 1 AND 2).
RX PubMed=27303034; DOI=10.1073/pnas.1522333113;
RA Kanemori Y., Koga Y., Sudo M., Kang W., Kashiwabara S., Ikawa M.,
RA Hasuwa H., Nagashima K., Ishikawa Y., Ogonuki N., Ogura A., Baba T.;
RT "Biogenesis of sperm acrosome is regulated by pre-mRNA alternative splicing
RT of Acrbp in the mouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:E3696-E3705(2016).
CC -!- FUNCTION: Acrosomal protein that maintains proacrosin (pro-ACR) as an
CC enzymatically inactive zymogen in the acrosome. Involved also in the
CC acrosome formation. {ECO:0000269|PubMed:27303034}.
CC -!- FUNCTION: [Acrosin-binding protein, mature form]: Maintains pro-ACR as
CC an enzymatically inactive zymogen in the acrosome until acrosomal
CC exocytosis (PubMed:27303034). Partially contributes also to the
CC assembly of acrosomal proteins to form an acrosomal granule
CC (PubMed:27303034). {ECO:0000269|PubMed:27303034}.
CC -!- FUNCTION: [Isoform 2]: Rodent specific isoform that participates in the
CC formation of the acrosomal granule into the center of the acrosomal
CC vesicle during early spermiogenesis (PubMed:27303034). In the
CC fertilization process promotes ACR release from the acrosome during
CC acrosomal exocytosis (PubMed:27303034). {ECO:0000269|PubMed:27303034}.
CC -!- SUBUNIT: [Acrosin-binding protein, mature form]: Binds pro-ACR. Does
CC not bind the mature form of ACR. {ECO:0000269|PubMed:23426433}.
CC -!- SUBUNIT: [Isoform 2]: Binds pro-ACR. Does not bind the mature form of
CC ACR. {ECO:0000269|PubMed:23426433}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasmic vesicle, secretory
CC vesicle, acrosome {ECO:0000269|PubMed:27303034}. Note=Colocalized with
CC pro-ACR in the acrosomal granules of early round spermatids.
CC {ECO:0000269|PubMed:23426433}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasmic vesicle, secretory
CC vesicle, acrosome {ECO:0000269|PubMed:22357636,
CC ECO:0000269|PubMed:23426433, ECO:0000269|PubMed:27303034}. Secreted
CC {ECO:0000250|UniProtKB:Q29016}. Note=Highly enriched in acrosomal
CC granules of round spermatids, and spread over the apical end of the
CC nucleus in elongating spermatids. Colocalized in the acrosome of
CC epididymal sperm with pro-ACR. {ECO:0000269|PubMed:23426433}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|Ref.1}; Synonyms=ACRBP-W
CC {ECO:0000303|PubMed:23426433};
CC IsoId=Q3V140-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|Ref.1}; Synonyms=ACRBP-V5
CC {ECO:0000303|PubMed:23426433};
CC IsoId=Q3V140-2; Sequence=VSP_051965, VSP_051966;
CC -!- TISSUE SPECIFICITY: [Isoform 1]: Testis-specific (at protein level).
CC Detected in pachytene spermatocytes and in haploid spermatids and in
CC elongating spermatids. {ECO:0000269|PubMed:22357636,
CC ECO:0000269|PubMed:23426433}.
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Testis-specific. Detected in pachytene
CC spermatocytes and round spermatids but absent in elongating spermatids.
CC Produced specifically in rodents. {ECO:0000269|PubMed:23426433}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000250|UniProtKB:Q29016}.
CC -!- PTM: Phosphorylated on Tyr residues in capacitated sperm.
CC {ECO:0000250|UniProtKB:Q29016}.
CC -!- PTM: [Isoform 1]: Synthesized as a 60-kDa precursor in pachytene
CC spermatocytes, postmeiotic spermatocytes and haploid spermatids and is
CC processed into the mature protein in elongating spermatids.
CC {ECO:0000269|PubMed:23426433}.
CC -!- PTM: [Isoform 2]: Degraded in elongating spermatid.
CC {ECO:0000269|PubMed:23426433}.
CC -!- DISRUPTION PHENOTYPE: Deficient male and female are normal in behavior,
CC body size, and health condition. Females exhibit normal fertility.
CC However, males exhibit a severely reduced fertility. The acrosomal
CC structure of spermatids is severely deformed at the later steps of
CC spermiogenesis. {ECO:0000269|PubMed:27303034}.
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DR EMBL; D17573; BAA04498.1; -; mRNA.
DR EMBL; D17574; BAA04499.1; -; mRNA.
DR EMBL; AK076691; BAC36445.1; -; mRNA.
DR EMBL; AK132705; BAE21313.1; -; mRNA.
DR EMBL; BC011079; AAH11079.1; -; mRNA.
DR CCDS; CCDS20542.1; -. [Q3V140-1]
DR CCDS; CCDS51910.1; -. [Q3V140-2]
DR RefSeq; NP_001120812.1; NM_001127340.1. [Q3V140-2]
DR RefSeq; NP_058541.2; NM_016845.2. [Q3V140-1]
DR AlphaFoldDB; Q3V140; -.
DR STRING; 10090.ENSMUSP00000085632; -.
DR iPTMnet; Q3V140; -.
DR PhosphoSitePlus; Q3V140; -.
DR MaxQB; Q3V140; -.
DR PaxDb; Q3V140; -.
DR PeptideAtlas; Q3V140; -.
DR PRIDE; Q3V140; -.
DR ProteomicsDB; 285940; -. [Q3V140-1]
DR ProteomicsDB; 285941; -. [Q3V140-2]
DR Antibodypedia; 48711; 91 antibodies from 21 providers.
DR DNASU; 54137; -.
DR Ensembl; ENSMUST00000088294; ENSMUSP00000085632; ENSMUSG00000072770. [Q3V140-1]
DR Ensembl; ENSMUST00000112414; ENSMUSP00000108033; ENSMUSG00000072770. [Q3V140-2]
DR GeneID; 54137; -.
DR KEGG; mmu:54137; -.
DR UCSC; uc009dth.1; mouse. [Q3V140-2]
DR UCSC; uc009dti.2; mouse. [Q3V140-1]
DR CTD; 84519; -.
DR MGI; MGI:1859515; Acrbp.
DR VEuPathDB; HostDB:ENSMUSG00000072770; -.
DR eggNOG; ENOG502R6TS; Eukaryota.
DR GeneTree; ENSGT00390000000826; -.
DR HOGENOM; CLU_879871_0_0_1; -.
DR InParanoid; Q3V140; -.
DR OMA; CPLCAFC; -.
DR OrthoDB; 961418at2759; -.
DR PhylomeDB; Q3V140; -.
DR TreeFam; TF336597; -.
DR BioGRID-ORCS; 54137; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Acrbp; mouse.
DR PRO; PR:Q3V140; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q3V140; protein.
DR Bgee; ENSMUSG00000072770; Expressed in skin of snout and 152 other tissues.
DR ExpressionAtlas; Q3V140; baseline and differential.
DR Genevisible; Q3V140; MM.
DR GO; GO:0002080; C:acrosomal membrane; ISS:UniProtKB.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0016504; F:peptidase activator activity; ISA:MGI.
DR GO; GO:0001675; P:acrosome assembly; IMP:UniProtKB.
DR GO; GO:0009566; P:fertilization; IMP:UniProtKB.
DR GO; GO:0007286; P:spermatid development; IMP:UniProtKB.
DR InterPro; IPR009865; Proacrosin-bd.
DR PANTHER; PTHR21362; PTHR21362; 1.
DR Pfam; PF07222; PBP_sp32; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasmic vesicle; Phosphoprotein;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..540
FT /note="Acrosin-binding protein"
FT /id="PRO_0000227517"
FT PROPEP 26..272
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:Q29016"
FT /id="PRO_0000449369"
FT CHAIN 273..540
FT /note="Acrosin-binding protein, mature form"
FT /id="PRO_0000449370"
FT REGION 26..105
FT /note="Pro-ACR binding"
FT /evidence="ECO:0000269|PubMed:23426433"
FT REGION 183..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..424
FT /note="Pro-ACR binding"
FT /evidence="ECO:0000269|PubMed:23426433"
FT COMPBIAS 194..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..232
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 312..316
FT /note="SLQQL -> RYRKL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|Ref.1"
FT /id="VSP_051965"
FT VAR_SEQ 317..540
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|Ref.1"
FT /id="VSP_051966"
FT CONFLICT 195
FT /note="R -> I (in Ref. 2; BAC36445)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="R -> H (in Ref. 1; BAA04498/BAA04499)"
FT /evidence="ECO:0000305"
FT CONFLICT 389
FT /note="L -> V (in Ref. 1; BAA04498)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 540 AA; 61141 MW; 14483661FF5884C4 CRC64;
MMNLAAGFLL MLLEVLLLPG TPLSAEESPA STPGSPLSST EYERFFALLT PTWKAETTCR
LRATHGCRNP TLVQLDQYEN HGLVPDGAVC SDLPYASWFE SFCQFAQYRC SNHVYYAKRV
RCSQPVSILS PNTLKEVESS AEVPPTSMTT PIVSHATATE HQAFQPWPER LNNNVEELLQ
SSLSLGGKDQ QSSRRPGQEQ RKQEQIQEHK LEEAQEQEEQ EEEEEEEEAK QEEGQGTEAG
LESVSRLQSD SEPKFQSQSL SSNPSFFTPR VREVESAPLM MKNIQELIRS AQEMDEMNEL
YDDSWRSQST GSLQQLPHME TLMVLCYSIM ENTCTMTPTA KAWSYMEEEI LGFGDSVCDN
LGRRHTAACP LCAFCSLKLE QCHSEASVLR QKCDASHKIP FISPLLSAQS ISTGNQARIP
DKGRFAGLEM YGGLSSEFWC NRLAMKGCED DRVSNWLKAE FLSFQEGDFP TKICDTNYIQ
YPNYCSFKSQ QCLLRNQNRK MSRMRCMLNE RYNVLSLAKS EEVILRWSQE FSTLAIGQFG
